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Q01594 (ALLN1_ALLSA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alliin lyase 1

Short name=Alliinase-1
EC=4.4.1.4
Alternative name(s):
Cysteine sulphoxide lyase 1
OrganismAllium sativum (Garlic)
Taxonomic identifier4682 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaAsparagalesAmaryllidaceaeAllioideaeAllieaeAllium

Protein attributes

Sequence length486 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Able to cleave the C-S bond of sulfoxide derivatives of Cys to produce allicin, thus giving rise to all sulfur compounds which are responsible for most of the properties of garlic, such as the specific smell and flavor as well as the health benefits like blood lipid or blood pressure lowering.

Catalytic activity

An S-alkyl-L-cysteine S-oxide = an alkyl sulfenate + 2-aminoacrylate.

Cofactor

Pyridoxal phosphate.

Subunit structure

Homodimer. Ref.3

Subcellular location

Vacuole.

Tissue specificity

Bulb and shoots.

Domain

The 6 Cys residues of the EGF-like domain are arranged in a disulfide pattern different from the one found in the canonical EGFs. The function of this domain is unclear. It may be a binding site for other proteins or the docking site for a putative alliinase receptor.

Sequence similarities

Belongs to the alliinase family.

Contains 1 EGF-like domain.

Ontologies

Keywords
   Cellular componentVacuole
   DomainEGF-like domain
Signal
   LigandChloride
Pyridoxal phosphate
   Molecular functionLyase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular_componentvacuole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionalliin lyase activity

Inferred from electronic annotation. Source: UniProtKB-EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Propeptide29 – 3810
PRO_0000020677
Chain39 – 486448Alliin lyase 1
PRO_0000020678

Regions

Domain51 – 9747EGF-like; atypical

Sites

Binding site1321Chloride
Binding site1361Chloride
Binding site1381Chloride

Amino acid modifications

Modified residue2891N6-(pyridoxal phosphate)lysine
Glycosylation571N-linked (GlcNAc...) Potential
Glycosylation1841N-linked (GlcNAc...)
Glycosylation2291N-linked (GlcNAc...) Potential
Glycosylation3661N-linked (GlcNAc...)
Disulfide bond58 ↔ 77
Disulfide bond79 ↔ 88
Disulfide bond82 ↔ 95
Disulfide bond406 ↔ 414

Secondary structure

......................................................................... 486
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q01594 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: D7862E867AD74383

FASTA48655,639
        10         20         30         40         50         60 
MVESYKKIGS CNKMPCLVIL TCIIMSNSLV NNNNMVQAKM TWTMKAAEEA EAVANINCSE 

        70         80         90        100        110        120 
HGRAFLDGII SEGSPKCECN TCYTGPDCSE KIQGCSADVA SGDGLFLEEY WKQHKEASAV 

       130        140        150        160        170        180 
LVSPWHRMSY FFNPVSNFIS FELEKTIKEL HEVVGNAAAK DRYIVFGVGV TQLIHGLVIS 

       190        200        210        220        230        240 
LSPNMTATPD APESKVVAHA PFYPVFREQT KYFNKKGYVW AGNAANYVNV SNPEQYIEMV 

       250        260        270        280        290        300 
TSPNNPEGLL RHAVIKGCKS IYDMVYYWPH YTPIKYKADE DILLFTMSKF TGHSGSRFGW 

       310        320        330        340        350        360 
ALIKDESVYN NLLNYMTKNT EGTPRETQLR SLKVLKEVVA MVKTQKGTMR DLNTFGFKKL 

       370        380        390        400        410        420 
RERWVNITAL LDQSDRFSYQ ELPQSEYCNY FRRMRPPSPS YAWVKCEWEE DKDCYQTFQN 

       430        440        450        460        470        480 
GRINTQNGVG FEASSRYVRL SLIKTQDDFD QLMYYLKDMV KAKRKTPLIK QLFIDQTETA 


SRRPFI 

« Hide

References

[1]"Isolation and characterization of alliinase cDNA clones from garlic (Allium sativum L.) and related species."
van Damme E.J.M., Smeets K., Torrekens S., van Leuven F., Peumans W.J.
Eur. J. Biochem. 209:751-757(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 39-58.
Tissue: Shoot.
[2]"Purification, characterization, and crystallization of alliinase from garlic."
Kuettner E.B., Hilgenfeld R., Weiss M.S.
Arch. Biochem. Biophys. 402:192-200(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, CRYSTALLIZATION.
Tissue: Bulb.
[3]"The active principle of garlic at atomic resolution."
Kuettner E.B., Hilgenfeld R., Weiss M.S.
J. Biol. Chem. 277:46402-46407(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 39-465, SUBUNIT.
Tissue: Bulb.
+Additional computationally mapped references.

Web resources

Protein Spotlight

What's that smell? - Issue 39 of October 2003

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z12622 mRNA. Translation: CAA78268.1.
PIRS29302.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LK9X-ray1.53A/B39-486[»]
2HORX-ray1.60A39-465[»]
2HOXX-ray1.40A/B/C/D39-465[»]
ProteinModelPortalQ01594.
SMRQ01594. Positions 39-465.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13504.

Family and domain databases

Gene3D2.10.25.30. 1 hit.
3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR006948. Alliinase_C.
IPR006947. EGF_alliinase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF04864. Alliinase_C. 1 hit.
PF04863. EGF_alliinase. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
PROSITEPS00022. EGF_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ01594.

Entry information

Entry nameALLN1_ALLSA
AccessionPrimary (citable) accession number: Q01594
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: April 16, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references